2rot: Difference between revisions
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==Structure of chimeric variant of SH3 domain- SHH== | |||
<StructureSection load='2rot' size='340' side='right'caption='[[2rot]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rot]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ROT FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rot OCA], [https://pdbe.org/2rot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rot RCSB], [https://www.ebi.ac.uk/pdbsum/2rot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rot ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2rot_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rot ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two chimeric proteins, SHcapital EN, Cyrillic and SHA of the "SH3-Bergerac" family (where the beta-turn N47D48 in spectrin SH3 domain was substituted for KITVNGKTYE or KATANGKTYE sequences, respectively), were analyzed by high-resolution NMR to resolve their spatial structures and to analyze their dynamics. Although the presence of a stable beta-hairpin in the region of the insertion was confirmed, the introduced extension of the polypeptide chain in SHcapital EN, Cyrillic (approximately 17%) practically did not affect the total molecule topology. Interestingly, the introduced beta-hairpin had higher mobility in comparison with other protein regions. Finally, we performed a disorder prediction with the PONDR VSL2 algorithm and discovered that the inserted beta-hairpin in both SHH and SHA proteins exhibited significant propensity for intrinsic disorder and therefore for high mobility. In agreement with the experimental data, the predisposition for the increased intramolecular mobility was noticeably higher in SHA. | |||
Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs".,Kutyshenko VP, Prokhorov DA, Timchenko MA, Kudrevatykh YA, Gushchina LV, Khristoforov VS, Filimonov VV, Uversky VN Biochim Biophys Acta. 2009 Dec;1794(12):1813-22. Epub 2009 Sep 2. PMID:19732853<ref>PMID:19732853</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2rot" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Spectrin|Spectrin]] | *[[Spectrin 3D structures|Spectrin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Filimonov | [[Category: Large Structures]] | ||
[[Category: Gushchina | [[Category: Filimonov VV]] | ||
[[Category: Khristoforov | [[Category: Gushchina LV]] | ||
[[Category: Kudrevatykh | [[Category: Khristoforov VS]] | ||
[[Category: Kutyshenko | [[Category: Kudrevatykh YA]] | ||
[[Category: Prokhorov | [[Category: Kutyshenko NP]] | ||
[[Category: Timchenko | [[Category: Prokhorov DA]] | ||
[[Category: Timchenko MA]] | |||
Latest revision as of 13:02, 14 June 2023
Structure of chimeric variant of SH3 domain- SHHStructure of chimeric variant of SH3 domain- SHH
Structural highlights
FunctionSPTN1_CHICK Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo chimeric proteins, SHcapital EN, Cyrillic and SHA of the "SH3-Bergerac" family (where the beta-turn N47D48 in spectrin SH3 domain was substituted for KITVNGKTYE or KATANGKTYE sequences, respectively), were analyzed by high-resolution NMR to resolve their spatial structures and to analyze their dynamics. Although the presence of a stable beta-hairpin in the region of the insertion was confirmed, the introduced extension of the polypeptide chain in SHcapital EN, Cyrillic (approximately 17%) practically did not affect the total molecule topology. Interestingly, the introduced beta-hairpin had higher mobility in comparison with other protein regions. Finally, we performed a disorder prediction with the PONDR VSL2 algorithm and discovered that the inserted beta-hairpin in both SHH and SHA proteins exhibited significant propensity for intrinsic disorder and therefore for high mobility. In agreement with the experimental data, the predisposition for the increased intramolecular mobility was noticeably higher in SHA. Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs".,Kutyshenko VP, Prokhorov DA, Timchenko MA, Kudrevatykh YA, Gushchina LV, Khristoforov VS, Filimonov VV, Uversky VN Biochim Biophys Acta. 2009 Dec;1794(12):1813-22. Epub 2009 Sep 2. PMID:19732853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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